Identification of a nonconserved amino acid residue in multidrug resistance protein 1 important for determining substrate specificity: evidence for functional interaction between transmembrane helices 14 and 17.
about
QacR−Cation Recognition Is Mediated by a Redundancy of Residues Capable of Charge Neutralization †A region within a lumenal loop of Saccharomyces cerevisiae Ycf1p directs proteolytic processing and substrate specificity.Cloning and characterization of the rat multidrug resistance-associated protein 1Molecular identification and characterization of rat Abcc1 cDNA: existence of two splicing variants and species difference in drug-resistance profileIntermediate structural states involved in MRP1-mediated drug transport. Role of glutathione.The human organic anion transporter 3 (OAT3; SLC22A8): genetic variation and functional genomics.The MRP family of drug efflux pumps.Functional Constraint Profiling of a Viral Protein Reveals Discordance of Evolutionary Conservation and FunctionalityModulation of oral drug bioavailability: from preclinical mechanism to therapeutic application.Substrate recognition and transport by multidrug resistance protein 1 (ABCC1).Transmembrane transport of endo- and xenobiotics by mammalian ATP-binding cassette multidrug resistance proteins.Determinants of the substrate specificity of multidrug resistance protein 1: role of amino acid residues with hydrogen bonding potential in predicted transmembrane helix 17.Functional importance of three basic residues clustered at the cytosolic interface of transmembrane helix 15 in the multidrug and organic anion transporter MRP1 (ABCC1).Functional importance of polar and charged amino acid residues in transmembrane helix 14 of multidrug resistance protein 1 (MRP1/ABCC1): identification of an aspartate residue critical for conversion from a high to low affinity substrate binding staMultiple membrane-associated tryptophan residues contribute to the transport activity and substrate specificity of the human multidrug resistance protein, MRP1.Substitution of Trp1242 of TM17 alters substrate specificity of human multidrug resistance protein 3.Photolabeling of human and murine multidrug resistance protein 1 with the high affinity inhibitor [125I]LY475776 and azidophenacyl-[35S]glutathione.Characterization of binding of leukotriene C4 by human multidrug resistance protein 1: evidence of differential interactions with NH2- and COOH-proximal halves of the protein.Characterization of the role of a highly conserved sequence in ATP binding cassette transporter G (ABCG) family in ABCG1 stability, oligomerization, and trafficking.GSH-dependent photolabeling of multidrug resistance protein MRP1 (ABCC1) by [125I]LY475776. Evidence of a major binding site in the COOH-proximal membrane spanning domain.Functional analysis of MRP1 cloned from bovine.S-decyl-glutathione nonspecifically stimulates the ATPase activity of the nucleotide-binding domains of the human multidrug resistance-associated protein, MRP1 (ABCC1).Charged amino acids in the sixth transmembrane helix of multidrug resistance protein 1 (MRP1/ABCC1) are critical determinants of transport activity.Structural and functional consequences of mutating cysteine residues in the amino terminus of human multidrug resistance-associated protein 1.Identification of domains participating in the substrate specificity and subcellular localization of the multidrug resistance proteins MRP1 and MRP2.
P2860
Q27651116-812C5BFD-3018-4AC2-986C-BC590AC589A0Q27938554-CB513360-87E0-4DF7-9C9F-F39254CB2C06Q28577126-3A3FCCF0-C7C2-4F51-B90C-92D79237353DQ28580674-ACB1299F-2FC8-45A5-9DEA-3408C27AD545Q34158355-159BEDFD-C804-4B0A-98FB-A06DD219B1A1Q34468094-2CEF631D-D5DB-44D7-9E25-8486889E5D5AQ35567296-18809773-3E5E-4727-9CBC-C26D0EBCB607Q35680145-DF22F21D-E74D-47F0-BC6A-02023DF9103EQ36271954-205D4927-B463-4760-AEE3-C31E74824B63Q36357541-BA5B6960-F210-4EB2-9998-919BC0075D6AQ36525551-3790B65F-0482-4018-9EA8-ABC69E936889Q38290639-8503D09D-0205-4425-A820-E094EDF94CC9Q40361067-FF2E8EB0-F4ED-491A-A2ED-C12A90EDE158Q40637908-012CEC54-30C5-450E-873C-E6ECDA6E6E70Q40696149-7AC7F76E-9099-4F02-9C1F-06717C02A0AAQ40696242-1D65C3FA-2C80-486D-A0AE-FAF96070192DQ40715791-FD208A73-1BA7-46A0-B386-14E3090D35BEQ40785860-F7E70A4E-BC1A-40B8-A81F-496911291868Q41849210-ED510F54-FE3C-490E-9D98-D9FB49F7047AQ44009278-AD962274-8D4D-4275-BC3C-B5CAADCC9245Q44030135-180EED7E-642B-4E6A-9064-2B2DAFB3497AQ44075217-5A63636C-7801-4DC9-B1EE-091E20BD338CQ44108486-E67A72FA-364D-4A9B-A0D0-F2A9557FB1BFQ44138744-4069424B-A8B9-4AF6-AAE5-8F79AB0ABBB9Q44394457-3F6776E5-5510-4052-8EF9-EE4190EEC01F
P2860
Identification of a nonconserved amino acid residue in multidrug resistance protein 1 important for determining substrate specificity: evidence for functional interaction between transmembrane helices 14 and 17.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh
2001年學術文章
@zh-hant
name
Identification of a nonconserv ...... ansmembrane helices 14 and 17.
@en
type
label
Identification of a nonconserv ...... ansmembrane helices 14 and 17.
@en
prefLabel
Identification of a nonconserv ...... ansmembrane helices 14 and 17.
@en
P2093
P2860
P356
P1476
Identification of a nonconserv ...... ansmembrane helices 14 and 17.
@en
P2093
P2860
P304
34966-34974
P356
10.1074/JBC.M105063200
P407
P577
2001-06-27T00:00:00Z